Observing biological dynamics at atomic resolution using NMR

被引:250
作者
Mittermaier, Anthony K. [1 ]
Kay, Lewis E. [2 ,3 ]
机构
[1] McGill Univ, Dept Chem, Montreal, PQ H3A 2K6, Canada
[2] Univ Toronto, Dept Chem, Toronto, ON M5S 1A8, Canada
[3] Univ Toronto, Dept Biochem & Mol Genet, Toronto, ON M5S 1A8, Canada
基金
加拿大健康研究院;
关键词
NUCLEAR-MAGNETIC-RESONANCE; RESIDUAL DIPOLAR COUPLINGS; MOLECULAR-WEIGHT PROTEINS; RELAXATION DISPERSION NMR; TIME-SCALE DYNAMICS; MODEL-FREE APPROACH; CHARACTERIZING CHEMICAL-EXCHANGE; MALTODEXTRIN-BINDING-PROTEIN; ORDER PARAMETERS; CONFORMATIONAL ENTROPY;
D O I
10.1016/j.tibs.2009.07.004
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Biological macromolecules are highly flexible and continually undergo conformational fluctuations on a broad spectrum of timescales. It has long been recognized that dynamics have an important role in the action of these molecules. However, the relationship between molecular function and motion is extremely challenging to delineate, because the conformational space available to macromolecules is vast and the relevant excursions can be infrequent and short-lived. Recent advances in solution nuclear magnetic resonance (NMR) spectroscopy permit biomolecular dynamics to be observed with unprecedented detail. Applications of these new NMR techniques to the study of fundamental processes such as binding and catalysis have provided new insights into how living systems operate at an atomic level.
引用
收藏
页码:601 / 611
页数:11
相关论文
共 91 条
[1]   NMR ORDER PARAMETERS AND FREE-ENERGY - AN ANALYTICAL APPROACH AND ITS APPLICATION TO COOPERATIVE CA2+ BINDING BY CALBINDIN-D(9K) [J].
AKKE, M ;
BRUSCHWEILER, R ;
PALMER, AG .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1993, 115 (21) :9832-9833
[2]   CARBON-13 FOURIER TRANFORM NUCLEAR MAGNETIC RESONANCE .3. CONFORMATION AND SEGMENTAL MOTION OF NATIVE AND DENATURED RIBONUCLEASE-A IN SOLUTION - APPLICATION OF NATURAL-ABUNDANCE CARBON-13 PARTIALLY RELAXED FOURIER TRANSFORM NUCLEAR MAGNETIC RESONANCE [J].
ALLERHAN.A ;
DODDRELL, D ;
GLUSHKO, U ;
COCHRAN, DW ;
WENKERT, E ;
LAWSON, PJ ;
GURD, FRN .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1971, 93 (02) :544-+
[3]   Protein folding pathways studied by pulsed-and native-state hydrogen exchange [J].
Bai, Yawen .
CHEMICAL REVIEWS, 2006, 106 (05) :1757-1768
[4]   Weak alignment NMR: a hawk-eyed view of biomolecular structure [J].
Bax, A ;
Grishaev, A .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 2005, 15 (05) :563-570
[5]   Paramagnetic probes in metalloproteins [J].
Bertini, I ;
Luchinat, C ;
Piccioli, M .
NUCLEAR MAGNETIC RESONANCE OF BIOLOGICAL MACROMOLECULES, PT B, 2001, 339 :314-340
[6]   The dynamic energy landscape of dihydrofolate reductase catalysis [J].
Boehr, David D. ;
McElheny, Dan ;
Dyson, H. Jane ;
Wright, Peter E. .
SCIENCE, 2006, 313 (5793) :1638-1642
[7]   Identification of slow correlated motions in proteins using residual dipolar and hydrogen-bond scalar couplings [J].
Bouvignies, G ;
Bernadó, P ;
Meier, S ;
Cho, K ;
Grzesiek, S ;
Brüschweiler, R ;
Blackledge, M .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2005, 102 (39) :13885-13890
[8]   Characterization of protein dynamics from residual dipolar couplings using the three dimensional Gaussian axial fluctuation model [J].
Bouvignies, Guillaume ;
Markwick, Phineus R. L. ;
Blackledge, Martin .
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2008, 71 (01) :353-363
[9]   Ubiquitin transfer from the E2 perspective - Why is UbcH5 so promiscuous? [J].
Brzovic, Peter S. ;
Klevit, Rachel E. .
CELL CYCLE, 2006, 5 (24) :2867-2873
[10]   PROTON MAGNETIC-RESONANCE STUDIES OF TYROSINE RESIDUES OF HEN LYSOZYME-ASSIGNMENT AND DETECTION OF CONFORMATIONAL MOBILITY [J].
CAMPBELL, ID ;
DOBSON, CM ;
WILLIAMS, RJP .
PROCEEDINGS OF THE ROYAL SOCIETY SERIES B-BIOLOGICAL SCIENCES, 1975, 189 (1097) :503-509